title: Deubiquitinating enzymes AtUBP12 and AtUBP13 and their tobacco homologue NtUBP12 are negative regulators of plant immunity.
abstract: • Signalling by ubiquitination is implicated in diverse aspects of the plant lifecycle, and enzymes of ubiquitin metabolism are overrepresented in the Arabidopsis genome compared with other model eukaryotes. Despite the importance of ubiquitination in the regulation of signalling, little is known about deubiquitinating enzymes, which reverse the process of ubiquitination. • Transgenic RNA interference-based cosuppression and the isolation of Atubp12/13 double mutants collectively provides the first report that AtUBP12 and AtUBP13 are functionally redundant and are required for immunity against virulent Pseudomonas syringae pv tomato in Arabidopsis. The Solanaceous AtUBP12 orthologue NtUBP12 was identified. Viral-induced gene silencing and transient gain-of-function assays were employed to establish that the NtUBP12 protein functions as a negative regulator of the Cf-9-triggered hypersensitive response. • Here, we demonstrate that NtUBP12 and AtUBP12 are bona fide deubiquitinating enzymes capable of cleaving lysine-48-linked ubiquitin chains. AtUBP12 and NtUBP12 are functionally interchangeable and their deubiquitinating activity is required to suppress plant cell death. • Overall, our data implicate AtUBP12- and NtUBP12-dependent deubiquitination in the stabilization of common substrates across Solanaceae and Brassicaceae which regulate disease resistance.
authors.affiliation: Biomedical and Life Sciences Department, University of Glasgow, Glasgow, G12 8QQ, UK.
authors.forename: Richard
authors.initials: R
authors.lastname: Ewan
authors.affiliation: Biomedical and Life Sciences Department, University of Glasgow, Glasgow, G12 8QQ, UK.
authors.forename: Ratih
authors.initials: R
authors.lastname: Pangestuti
authors.affiliation: School of Life Sciences, University of Warwick, Wellesbourne, CV35 9EF, UK.
authors.forename: Sarah
authors.initials: S
authors.lastname: Thornber
authors.affiliation: School of Life Sciences, University of Warwick, Wellesbourne, CV35 9EF, UK.
authors.forename: Adam
authors.initials: A
authors.lastname: Craig
authors.affiliation: Biomedical and Life Sciences Department, University of Glasgow, Glasgow, G12 8QQ, UK.
authors.forename: Craig
authors.initials: C
authors.lastname: Carr
authors.affiliation: Biomedical and Life Sciences Department, University of Glasgow, Glasgow, G12 8QQ, UK.
authors.forename: Liz
authors.initials: L
authors.lastname: O'Donnell
authors.affiliation: School of Life Sciences, University of Warwick, Wellesbourne, CV35 9EF, UK.
authors.forename: Cunjn
authors.initials: C
authors.lastname: Zhang
authors.affiliation: Biomedical and Life Sciences Department, University of Glasgow, Glasgow, G12 8QQ, UK.|School of Life Sciences, University of Warwick, Wellesbourne, CV35 9EF, UK.
authors.forename: Ari
authors.initials: A
authors.lastname: Sadanandom
mesh_terms: D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000201:enzymology* / Q000276:immunology / Q000382:microbiology; D029681:Arabidopsis Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D010450:Endopeptidases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D007113:Immunity, Innate / Q000235:genetics; D008562:Membrane Glycoproteins / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D009154:Mutation; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D044224:Pseudomonas syringae / Q000276:immunology; D034622:RNA Interference; D016415:Sequence Alignment; D015398:Signal Transduction; D014026:Nicotiana / Q000201:enzymology* / Q000276:immunology / Q000382:microbiology; D064570:Ubiquitin-Specific Proteases; D054875:Ubiquitination
chemical_list: D029681:Arabidopsis Proteins; C109609:Cf protein, Lycopersicon esculentum; D008562:Membrane Glycoproteins; D010940:Plant Proteins; D010450:Endopeptidases; D064570:Ubiquitin-Specific Proteases; C561399:UBP12 protein, Arabidopsis; C561400:UBP13 protein, Arabidopsis